Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles (Q27938340)

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Language	Label	Description	Also known as
English	Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles	scientific article

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scholarly article

1 reference

PubMed publication ID

1 December 2016

Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles (English)

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PubMed publication ID

1 December 2016

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GOA release 2020-03-11

Protein-arginine omega-N methyltransferase HMT1 YBR034C

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GOA release 2020-03-11

MRNA-binding translational repressor SSD1 YDR293C

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GOA release 2020-03-11

MRNA-binding protein NPL3 YDR432W

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GOA release 2020-03-11

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GOA release 2020-03-11

SWI/SNF catalytic subunit SNF2 YOR290C

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GOA release 2020-03-11

ATP-dependent RNA helicase MTR4 YJL050W

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GOA release 2020-03-11

author name string

Christopher A Jackson

1

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Neelu Yadav

2

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Sangwon Min

3

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Jun Li

4

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Eric J Milliman

5

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Jun Qu

6

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Yin-Chu Chen

7

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Michael C Yu

8

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language of work or name

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publication date

November 2012

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1 reference

PubMed publication ID

1 December 2016

12

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22

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3304-14

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Protein arginine methylation in mammals: who, what, and why

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Protein arginine methyltransferases: from unicellular eukaryotes to humans

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Effects of asymmetric arginine dimethylation on RNA-binding peptides

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors.

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Arginine methylation of REF/ALY promotes efficient handover of mRNA to TAP/NXF1.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Methylation of histone H3 by coactivator-associated arginine methyltransferase 1

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae

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https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

The role of protein arginine methylation in the formation of silent chromatin

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

A proteomic analysis of arginine-methylated protein complexes

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Methylation of SPT5 Regulates Its Interaction with RNA Polymerase II and Transcriptional Elongation Properties

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

MeMo: a web tool for prediction of protein methylation modifications.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Identification of protein methylation sites by coupling improved ant colony optimization algorithm and support vector machine

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Incorporating structural characteristics for identification of protein methylation sites

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Computational identification of protein methylation sites through bi-profile Bayes feature extraction

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Asymmetric arginine dimethylation determines life span in C. elegans by regulating forkhead transcription factor DAF-16.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

A generic protein purification method for protein complex characterization and proteome exploration

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

A straightforward and highly efficient precipitation/on-pellet digestion procedure coupled with a long gradient nano-LC separation and Orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Combinatorial peptide ligand library treatment followed by a dual-enzyme, dual-activation approach on a nanoflow liquid chromatography/orbitrap/electron transfer dissociation system for comprehensive analysis of swine plasma proteome.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Ultrasensitive quantification of serum vitamin D metabolites using selective solid-phase extraction coupled to microflow liquid chromatography and isotope-dilution mass spectrometry.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Electron transfer dissociation coupled to an Orbitrap analyzer may promise a straightforward and accurate sequencing of disulfide‐bridged cyclic peptides: a case study

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Arginine methylation facilitates the nuclear export of hnRNP proteins

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

The Ccr4-Not complex interacts with the mRNA export machinery

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

RNA degradation by the exosome is promoted by a nuclear polyadenylation complex

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

A multisubunit complex containing the SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated from yeast

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Control of replication initiation and heterochromatin formation in Saccharomyces cerevisiae by a regulator of meiotic gene expression

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

The Bre5/Ubp3 ubiquitin protease complex from budding yeast contributes to the cellular response to DNA damage

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Nucleocytoplasmic shuttling of Ssd1 defines the destiny of its bound mRNAs

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Functional organization of the yeast proteome by systematic analysis of protein complexes

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network.

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

The yeast SNF2/SWI2 protein has DNA-stimulated ATPase activity required for transcriptional activation

1 reference

https://api.crossref.org/works/10.1002%2FPMIC.201200132

21 January 2018

Identifiers

10.1002/PMIC.201200132

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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